ID G1ERE1_9NEOP Unreviewed; 962 AA.
AC G1ERE1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Pyrimidine biosynthesis {ECO:0000313|EMBL:AEM24215.1};
DE Flags: Fragment;
OS Caloptilia obliquatella.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC Gracillariidae; Caloptilia.
OX NCBI_TaxID=1075125 {ECO:0000313|EMBL:AEM24215.1};
RN [1] {ECO:0000313|EMBL:AEM24215.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21702958; DOI=10.1186/1471-2148-11-182;
RA Kawahara A.Y., Ohshima I., Kawakita A., Regier J.C., Mitter C.,
RA Cummings M.P., Davis D.R., Wagner D.L., De Prins J., Lopez-Vaamonde C.;
RT "Increased gene sampling strengthens support for higher-level groups within
RT leaf-mining moths and relatives (Lepidoptera: Gracillariidae).";
RL BMC Evol. Biol. 11:182-182(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
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DR EMBL; JN125084; AEM24215.1; -; mRNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 468..660
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEM24215.1"
FT NON_TER 962
FT /evidence="ECO:0000313|EMBL:AEM24215.1"
SQ SEQUENCE 962 AA; 107024 MW; 0A103644A833C334 CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD EGEKDEHGLP KWFESNRIWA AGLIVGEVST
KAWHWRAKKS LGNWLAAYGV PGVCEVDTRA LTRKLRXGVT LGRIVQGAPP IADPNTRNLV
AEVSIKEPKV YNENGSFTIM AIDCGLKYNQ IRCLIKRNAK VILVPWNYPL DPTKYDGLFI
SNGPGDPDMC XNTVQNIKTV LKPVFGICLG HQLLSTAVGC HTFKMSYGNR GHNLPCTHSE
TGRCYMTSQN HGFAVDTXTL PKDWKLLFTN ENDKTNEGVI HETLPYFSVQ FHPEHTAGPT
DLELLFDVFV DAVKTYKRGE KCIVNSMITE RLHFVPTLQE RPKKVLILGS GGLSIGQAGE
FDYSGSQAVK AMQEEKILTV LINPNIATVQ TSKGLADKVY FLPITPEYVE QVIKAERPTG
VLLTFGGQTA LNCGVELKKS GVFEKYNVNV LGTPIQSIID TEDRKIFAEK INFIGEKVAP
SAAVSSVEEA LVAANQIGYP VMARAAFSLG GLGSGFANNE DELKILAQQA FAHSDQLIID
KSLKGWKEVE YEVVRDAFDN CITVCNMENV DPLGIHTGES IVVAPSQTLS NREYYMLRNT
AIKVIRHFGI VGECNIQYAL NPYSEEFYII EVNARLSRSS ALASKATGYP LAYVAAKLAL
GVPLPKIKNS VTGVTTACFE PSLDYCVVKI PRWDLAKFNR VSTKIGSSMK SVGEVMSIGR
NFEEAFQKAL RMVDENVTGF DPTIKKVNDX ELREPTDKRM FVLAAALREG YTIEKLYELT
KIDRWFLQKL KNITDHYVVL GNQGVISIEN LKKSKQMGFS DKQIAAAIKS TEIAVRKLRD
QNKIXPFVKQ IDTVAAEWPA TTNYLYLTYN GISHDIEFPG EFTMVLGSGV YRIGSSVEFD
WCAVGCLREL RRQGKQTIMI NYNPETVSTD YDMSDRLYFE EISFEVVMDI YNLEKPDGVI
LS
//
